Cited by 93Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesCell Adhesion Molecules Research

p130Cas: A key signalling node in health and disease

Barrett, Angela, Pellet-Many, Caroline, Zachary, Ian C., Evans, Ian M., Frankel, Paul·2013·Cellular Signalling

Abstract

p130Cas/breast cancer anti-oestrogen resistance 1 (BCAR1) is a member of the Cas (Crk-associated substrate) family of adaptor proteins, which have emerged as key signalling nodes capable of interactions with multiple proteins, with important regulatory roles in normal and pathological cell function. The Cas family of proteins is characterised by the presence of multiple conserved motifs for protein-protein interactions, and by extensive tyrosine and serine phosphorylations. Recent studies show that p130Cas contributes to migration, cell cycle control and apoptosis. p130Cas is essential during early embryogenesis, with a critical role in cardiovascular development. Furthermore, p130Cas has been reported to be involved in the development and progression of several human cancers. p130Cas is able to perform roles in multiple processes due to its capacity to regulate a diverse array of signalling pathways, transducing signals from growth factor receptor tyrosine kinases, non-receptor tyrosine kinases, and integrins. In this review we summarise the current understanding of the structure, function, and regulation of p130Cas, and discuss the importance of p130Cas in both physiological and pathophysiological settings, with a focus on the cardiovascular system and cancer.

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Crossref · 10.1016/j.cellsig.2012.12.019

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  • Little is currently known about CASS4 biology or its role in neurological health and disease.

    “Despite CASS4 being increasingly linked to AD risk in humans (EADB et al., 2026; Lambert et al., 2013; Lin et al., 2017; Ramos de Matos et al., 2018; Schwartzentruber et al., 2021; Wang et al., 2015b), little is currently known about CASS4 biology or its role in neurological health and disease.”
  • PTK2B encodes the protein PYK2 and is a suggested CASS4-binding partner.

    “Moreover, mutations in the focal adhesion gene PTK2B , which encodes the protein PYK2 and is a suggested CASS4binding partner (Barrett et al., 2013; Beck et al., 2014), have also been linked to increased AD risk in GWAS studies (Lambert et al., 2013; Lin et al., 2017; Ramos de Matos et al., 2018; Schwartzentruber et al., 2021; Wang et al., 2015b).”

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Authors
Barrett, A., Pellet-Many, C., Zachary, I. C., Evans, I. M., & Frankel, P.
Affiliations
University College London (GB)
Corresponding author
  • Barrett, Angela
  • Frankel, Paul
Venue
Cellular Signalling
Publisher
Elsevier BV
Published
2013-04
Volume
25
Issue
4
Pages
766-777
ISSN
0898-6568 (ISSN-L)
OpenAlex
W2126859572
Cited by
93
References
5
Citations by year
2026: 3 · 2025: 7 · 2024: 11 · 2023: 5 · 2022: 3 · 2021: 8 · 2020: 9 · 2019: 5 · 2018: 6 · 2017: 4 · 2016: 7 · 2015: 13 · 2014: 10 · 2013: 2
FWCI
0.73
Type
journal article
Language
en
Open access
closed
Locations
  • Cellular Signalling (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Funders
British Heart Foundation (RG/11/11/29050, RG/06/003/21131)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords
p130Cas, adaptor proteins, protein-protein interaction, tyrosine phosphorylation, serine phosphorylation, cell migration, cell cycle regulation, apoptosis, embryonic development, cardiovascular development, tumor progression, growth factor receptor tyrosine kinases, non-receptor tyrosine kinase, integrins, signal transduction
MeSH terms
Cardiovascular System, Humans, Neoplasms, Phosphorylation, Signal Transduction, Guanine Nucleotide Exchange Factors, Mechanotransduction, Cellular, Crk-Associated Substrate Protein

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